title: The perturbation of tryptophan fluorescence by phenylalanine to alanine mutations identifies the hydrophobic core in a subset of bacterial Ig-like domains.
abstract: Many host-parasite interactions are mediated via surface-exposed proteins containing bacterial immunoglobulin-like (Big) domains. Here, we utilize the spectral properties of a conserved Trp to provide evidence that, along with a Phe, these residues are positioned within the hydrophobic core of a subset of Big_2 domains. The mutation of the Phe to Ala decreases Big_2 domain stability and impairs the ability of LigBCen2 to bind to the host protein, fibronectin.
authors.affiliation: Centre for Cellular and Molecular Biology (CCMB), CSIR , Uppal Road, Hyderabad 500 007, India.
authors.forename: Rajeev
authors.initials: R
authors.lastname: Raman
authors.forename: Christopher P
authors.initials: CP
authors.lastname: Ptak
authors.forename: Ching-Lin
authors.initials: CL
authors.lastname: Hsieh
authors.forename: Robert E
authors.initials: RE
authors.lastname: Oswald
authors.forename: Yung-Fu
authors.initials: YF
authors.lastname: Chang
authors.forename: Yogendra
authors.initials: Y
authors.lastname: Sharma
mesh_terms: D000409:Alanine / Q000737:chemistry*; D001173:Arthrobacter / Q000737:chemistry*; D005453:Fluorescence; D057927:Hydrophobic and Hydrophilic Interactions; D007136:Immunoglobulins / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry*; D014364:Tryptophan / Q000737:chemistry*
chemical_list: D007136:Immunoglobulins; D010649:Phenylalanine; D014364:Tryptophan; D000409:Alanine